Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-7-26
pubmed:abstractText
Pulmonary surfactant protein A (SP-A) is an oligomeric collectin that recognizes lipid and carbohydrate moieties present on broad range of micro-organisms, and mediates microbial lysis and clearance. SP-A also modulates multiple immune-related functions including cytokine production and chemotaxis for phagocytes. Here we describe the molecular interaction between the extracellular matrix protein microfibril-associated protein 4 (MFAP4) and SP-A. MFAP4 is a collagen-binding molecule containing a C-terminal fibrinogen-like domain and a N-terminal located integrin-binding motif. We produced recombinant MFAP4 with a molecular mass of 36 and 66 kDa in the reduced and unreduced states respectively. Gel filtration chromatography and chemical crosslinking showed that MFAP4 forms oligomers of four dimers. We demonstrated calcium-dependent binding between MFAP4 and human SP-A1 and SP-A2. No binding was seen to recombinant SP-A composed of the neck region and carbohydrate recognition domain of SP-A indicating that the interaction between MFAP4 and SP-A is mediated via the collagen domain of SP-A. Monoclonal antibodies directed against MFAP4 and SP-A were used for immunohistochemical analysis, which demonstrates that the two molecules colocalize both on the elastic fibres in the interalveolar septum and in elastic lamina of pulmonary arteries of chronically inflamed lung tissue. We conclude, that MFAP4 interacts with SP-A via the collagen region in vitro, and that MFAP4 and SP-A colocates in different lung compartments indicating that the interaction may be operative in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0300-9475
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-16
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16867155-Animals, pubmed-meshheading:16867155-Binding Sites, pubmed-meshheading:16867155-Blotting, Western, pubmed-meshheading:16867155-Bronchoalveolar Lavage Fluid, pubmed-meshheading:16867155-CHO Cells, pubmed-meshheading:16867155-Calcium, pubmed-meshheading:16867155-Carrier Proteins, pubmed-meshheading:16867155-Cricetinae, pubmed-meshheading:16867155-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:16867155-Extracellular Matrix, pubmed-meshheading:16867155-Extracellular Matrix Proteins, pubmed-meshheading:16867155-Glycoproteins, pubmed-meshheading:16867155-Humans, pubmed-meshheading:16867155-Immunohistochemistry, pubmed-meshheading:16867155-Lung, pubmed-meshheading:16867155-Microscopy, Immunoelectron, pubmed-meshheading:16867155-Protein Binding, pubmed-meshheading:16867155-Pulmonary Surfactant-Associated Protein A, pubmed-meshheading:16867155-Recombinant Proteins
pubmed:year
2006
pubmed:articleTitle
Microfibril-associated protein 4 binds to surfactant protein A (SP-A) and colocalizes with SP-A in the extracellular matrix of the lung.
pubmed:affiliation
Medical Biotechnology Center, University of Southern Denmark, Odense, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't